RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
- Ju-Yuan Zhang1,
- Xue-Mei Deng1,
- Feng-Pu Li1,
- Li Wang1,
- Qiao-Yun Huang1,
- Cheng-Cai Zhang2 and
- Wen-Li Chen1,3
- 1National Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China
- 2Aix-Marseille Université and CNRS, Laboratoire de Chimie Bactérienne–UMR7283, 13402 Marseille cedex 20, France
Abstract
RNase E, a central component involved in bacterial RNA metabolism, usually has a highly conserved N-terminal catalytic domain but an extremely divergent C-terminal domain. While the C-terminal domain of RNase E in Escherichia coli recruits other components to form an RNA degradation complex, it is unknown if a similar function can be found for RNase E in other organisms due to the divergent feature of this domain. Here, we provide evidence showing that RNase E forms a complex with another essential ribonuclease—the polynucleotide phosphorylase (PNPase)—in cyanobacteria, a group of ecologically important and phylogenetically ancient organisms. Sequence alignment for all cyanobacterial RNase E proteins revealed several conserved and variable subregions in their noncatalytic domains. One such subregion, an extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena PCC7120 and the unicellular cyanobacterium Synechocystis PCC6803. These results indicate that RNase E and PNPase form a ribonuclease complex via a common mechanism in cyanobacteria. The PNPase-recognition motif in cyanobacterial RNase E is distinct from those previously identified in Proteobacteria, implying a mechanism of coevolution for PNPase and RNase E in different organisms.
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↵3 Corresponding author
E-mail wlchen{at}mail.hzau.edu.cn
- Received November 15, 2013.
- Accepted January 23, 2014.
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